(data stored in ACNUC7421 zone)

SWISSPROT: Q147A5_PARXL

ID   Q147A5_PARXL            Unreviewed;       167 AA.
AC   Q147A5;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 87.
DE   RecName: Full=Peptide deformylase {ECO:0000256|HAMAP-Rule:MF_00163, ECO:0000256|SAAS:SAAS01077920};
DE            Short=PDF {ECO:0000256|HAMAP-Rule:MF_00163};
DE            EC=3.5.1.88 {ECO:0000256|HAMAP-Rule:MF_00163, ECO:0000256|SAAS:SAAS01077920};
DE   AltName: Full=Polypeptide deformylase {ECO:0000256|HAMAP-Rule:MF_00163};
GN   Name=def {ECO:0000256|HAMAP-Rule:MF_00163};
GN   ORFNames=Bxe_A4416 {ECO:0000313|EMBL:ABE28584.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28584.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28584.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28584.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Removes the formyl group from the N-terminal Met of
CC       newly synthesized proteins. Requires at least a dipeptide for an
CC       efficient rate of reaction. N-terminal L-methionine is a
CC       prerequisite for activity but the enzyme has broad specificity at
CC       other positions. {ECO:0000256|HAMAP-Rule:MF_00163}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate
CC         + N-terminal L-methionyl-[peptide]; Xref=Rhea:RHEA:24420,
CC         Rhea:RHEA-COMP:10639, Rhea:RHEA-COMP:10640, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:49298, ChEBI:CHEBI:64731;
CC         EC=3.5.1.88; Evidence={ECO:0000256|HAMAP-Rule:MF_00163,
CC         ECO:0000256|SAAS:SAAS01115621};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00163};
CC       Note=Binds 1 Fe(2+) ion. {ECO:0000256|HAMAP-Rule:MF_00163};
CC   -!- SIMILARITY: Belongs to the polypeptide deformylase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00163, ECO:0000256|SAAS:SAAS01077936}.
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DR   EMBL; CP000270; ABE28584.1; -; Genomic_DNA.
DR   RefSeq; WP_011486442.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A4416; -.
DR   EnsemblBacteria; ABE28584; ABE28584; Bxe_A4416.
DR   GeneID; 4002024; -.
DR   KEGG; bxb:DR64_2091; -.
DR   KEGG; bxe:Bxe_A4416; -.
DR   PATRIC; fig|266265.5.peg.48; -.
DR   eggNOG; ENOG4108Z02; Bacteria.
DR   eggNOG; COG0242; LUCA.
DR   HOGENOM; HOG000243509; -.
DR   KO; K01462; -.
DR   OMA; VCIQHEI; -.
DR   OrthoDB; 1649129at2; -.
DR   BioCyc; BXEN266265:BXE_RS00230-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042586; F:peptide deformylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00487; Pep_deformylase; 1.
DR   Gene3D; 3.90.45.10; -; 1.
DR   HAMAP; MF_00163; Pep_deformylase; 1.
DR   InterPro; IPR023635; Peptide_deformylase.
DR   InterPro; IPR036821; Peptide_deformylase_sf.
DR   PANTHER; PTHR10458; PTHR10458; 1.
DR   Pfam; PF01327; Pep_deformylase; 1.
DR   PIRSF; PIRSF004749; Pep_def; 1.
DR   PRINTS; PR01576; PDEFORMYLASE.
DR   SUPFAM; SSF56420; SSF56420; 1.
DR   TIGRFAMs; TIGR00079; pept_deformyl; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q147A5.
DR   SWISS-2DPAGE; Q147A5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00163,
KW   ECO:0000256|SAAS:SAAS01077916, ECO:0000313|EMBL:ABE28584.1};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00163};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00163,
KW   ECO:0000256|SAAS:SAAS01077917};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00163,
KW   ECO:0000256|SAAS:SAAS01077930};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   ACT_SITE    135    135       {ECO:0000256|HAMAP-Rule:MF_00163}.
FT   METAL        92     92       Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.
FT   METAL       134    134       Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.
FT   METAL       138    138       Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.
SQ   SEQUENCE   167 AA;  19017 MW;  9D35727DAD3ACEF1 CRC64;
     MALLNIINYP DKRLHKIAKP VEAVNDRIRR LVKDMAETMY AAPGVGLAAT QVDVHERVIV
     IDVSDDHNEL LTFINPEIIW SSDERKLSEE GCLSVPGIYD NVERAEKVRV RALNEKGETF
     EMDCEGLLAV CIQHEMDHLM GRVFVEYLSS LKQTRIKSKM KKLAHAM
//

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